ID   HTRSN_PHYTS             Reviewed;          24 AA.
AC   P84337;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Homotarsinin {ECO:0000303|Ref.1};
OS   Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=306084;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AMIDATION AT ARG-24, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion {ECO:0000303|Ref.1};
RA   Prates M.V., Santos N.C.F., Leite J.R.S.A., Figueredo R.C.R., Martins G.R.,
RA   Bloch C. Jr.;
RT   "Homotarsinin: A novel antimicrobial homodimer peptide from skin secretion
RT   of Phyllomedusa tarsius (Amphibia).";
RL   Submitted (DEC-2004) to UniProtKB.
RN   [2] {ECO:0000305}
RP   STRUCTURE BY NMR OF 1-24, FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-23.
RX   PubMed=28102305; DOI=10.1038/srep40854;
RA   Verly R.M., Resende J.M., Junior E.F., de Magalhaes M.T., Guimaraes C.F.,
RA   Munhoz V.H., Bemquerer M.P., Almeida F.C., Santoro M.M., Pilo-Veloso D.,
RA   Bechinger B.;
RT   "Structure and membrane interactions of the homodimeric antibiotic peptide
RT   homotarsinin.";
RL   Sci. Rep. 7:40854-40854(2017).
CC   -!- FUNCTION: Antimicrobial peptide (Ref.1, PubMed:28102305). Active
CC       against Gram-negative bacteria E.coli ATCC 25922 (MIC=1.5 uM) and
CC       P.aeruginosa ATTC 27853 (MIC=23.2 uM) and against Gram-positive
CC       bacterium S.aureus ATCC 29313 (MIC=11.6 uM) (Ref.1, PubMed:28102305).
CC       Has no hemolytic activity (Ref.1). Associates with and disrupts
CC       membranes in vitro (PubMed:28102305). {ECO:0000269|PubMed:28102305,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:28102305,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000305|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=5503.85; Mass_error=0.5; Method=MALDI;
CC       Note=Homodimer.; Evidence={ECO:0000269|Ref.1};
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DR   PDB; 6WUX; NMR; -; A/B=1-24.
DR   PDB; 7MN3; NMR; -; A=1-24.
DR   PDBsum; 6WUX; -.
DR   PDBsum; 7MN3; -.
DR   AlphaFoldDB; P84337; -.
DR   SMR; P84337; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Secreted.
FT   PEPTIDE         1..24
FT                   /note="Homotarsinin"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000440097"
FT   MOD_RES         24
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|Ref.1"
FT   DISULFID        23
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:28102305, ECO:0000269|Ref.1"
FT   MUTAGEN         23
FT                   /note="C->S: Loss of dimerization."
FT                   /evidence="ECO:0000269|PubMed:28102305"
FT   HELIX           4..20
FT                   /evidence="ECO:0007829|PDB:6WUX"
SQ   SEQUENCE   24 AA;  2754 MW;  1AB1B4207AC9E567 CRC64;
     NLVSDIIGSK KHMEKLISII KKCR